2hzd
From Proteopedia
(New page: 200px<br /> <applet load="2hzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hzd" /> '''NMR structure of the DNA-binding TEA domain...) |
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'''NMR structure of the DNA-binding TEA domain and insights into TEF-1 function'''<br /> | '''NMR structure of the DNA-binding TEA domain and insights into TEF-1 function'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Transcription enhancer factor 1 is essential for cardiac, skeletal, and | + | Transcription enhancer factor 1 is essential for cardiac, skeletal, and smooth muscle development and uses its N-terminal TEA domain (TEAD) to bind M-CAT elements. Here, we present the first structure of TEAD and show that it is a three-helix bundle with a homeodomain fold. Structural data reveal how TEAD binds DNA. Using structure-function correlations, we find that the L1 loop is essential for cooperative loading of TEAD molecules on to tandemly duplicated M-CAT sites. Furthermore, using a microarray chip-based assay, we establish that known binding sites of the full-length protein are only a subset of DNA elements recognized by TEAD. Our results provide a model for understanding the regulation of genome-wide gene expression during development by TEA/ATTS family of transcription factors. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2HZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HZD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:47:28 2008'' |
Revision as of 15:47, 21 February 2008
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NMR structure of the DNA-binding TEA domain and insights into TEF-1 function
Contents |
Overview
Transcription enhancer factor 1 is essential for cardiac, skeletal, and smooth muscle development and uses its N-terminal TEA domain (TEAD) to bind M-CAT elements. Here, we present the first structure of TEAD and show that it is a three-helix bundle with a homeodomain fold. Structural data reveal how TEAD binds DNA. Using structure-function correlations, we find that the L1 loop is essential for cooperative loading of TEAD molecules on to tandemly duplicated M-CAT sites. Furthermore, using a microarray chip-based assay, we establish that known binding sites of the full-length protein are only a subset of DNA elements recognized by TEAD. Our results provide a model for understanding the regulation of genome-wide gene expression during development by TEA/ATTS family of transcription factors.
Disease
Known disease associated with this structure: Sveinsson choreoretinal atrophy OMIM:[189967]
About this Structure
2HZD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain., Anbanandam A, Albarado DC, Nguyen CT, Halder G, Gao X, Veeraraghavan S, Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17225-30. Epub 2006 Nov 3. PMID:17085591
Page seeded by OCA on Thu Feb 21 17:47:28 2008
